Journal of Biological Chemistry
Enzyme Catalysis and RegulationStructural and Kinetic Evidence for an Extended Hydrogen-bonding Network in Catalysis of Methyl Group Transfer: ROLE OF AN ACTIVE SITE ASPARAGINE RESIDUE IN ACTIVATION OF METHYL TRANSFER BY METHYLTRANSFERASES*♦
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This paper is dedicated to Professor Martha Ludwig, who passed away on November 27, 2006. Martha was a thoughtful, thorough, and innovative scientist who made extremely important contributions to our understanding of the structure and function of cobalamin-dependent methyltransferases. Martha was a crystallographer who was a faculty member in the Biological Chemistry Department at the University of Michigan for almost 40 years and a member of the National Academy of Sciences and of the Institute of Medicine. She also was a caring friend who we wish could have seen this paper in print.
The atomic coordinates and structure factors (codes 2E7F and 2OGY) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).
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The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
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This article was selected as a Paper of the Week.
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Both authors contributed equally to the publication (alphabetical order).
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Present Address: Stanford Linear Accelerator Center, 2575 Sand Hill Rd., Menlo Park, CA 94025.
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Present Address: Dept. of Applied Molecular Bioscience, Nagoya University, Graduate School of Bioagricultural Sciences, Furo-Cho, Chikusa-Ku, Nagoya 464-8601, Japan.